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Magnesium in PDB 2cnq: Atomic Resolution Structure of Saicar-Synthase From Saccharomyces Cerevisiae Complexed with Adp, Aicar, Succinate

Enzymatic activity of Atomic Resolution Structure of Saicar-Synthase From Saccharomyces Cerevisiae Complexed with Adp, Aicar, Succinate

All present enzymatic activity of Atomic Resolution Structure of Saicar-Synthase From Saccharomyces Cerevisiae Complexed with Adp, Aicar, Succinate:
6.3.2.6;

Protein crystallography data

The structure of Atomic Resolution Structure of Saicar-Synthase From Saccharomyces Cerevisiae Complexed with Adp, Aicar, Succinate, PDB code: 2cnq was solved by D.V.Urusova, S.V.Antonyuk, A.I.Grebenko, V.M.Levdikov, V.V.Barynin, A.N.Popov, V.S.Lamzin, W.R.Melik-Adamyan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.00 / 1.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.683, 61.851, 76.893, 90.00, 90.00, 90.00
R / Rfree (%) 11.5 / 13

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Atomic Resolution Structure of Saicar-Synthase From Saccharomyces Cerevisiae Complexed with Adp, Aicar, Succinate (pdb code 2cnq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Atomic Resolution Structure of Saicar-Synthase From Saccharomyces Cerevisiae Complexed with Adp, Aicar, Succinate, PDB code: 2cnq:

Magnesium binding site 1 out of 1 in 2cnq

Go back to Magnesium Binding Sites List in 2cnq
Magnesium binding site 1 out of 1 in the Atomic Resolution Structure of Saicar-Synthase From Saccharomyces Cerevisiae Complexed with Adp, Aicar, Succinate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Atomic Resolution Structure of Saicar-Synthase From Saccharomyces Cerevisiae Complexed with Adp, Aicar, Succinate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1314

b:7.8
occ:1.00
 O1B A:ADP1307 2.0 9.7 1.0
O A:HOH2538 2.0 8.6 1.0
O A:HOH2670 2.0 10.9 1.0
O A:HOH2518 2.0 7.4 1.0
O1A A:ADP1307 2.1 7.4 1.0
O A:HOH2684 2.1 10.3 0.9
PB A:ADP1307 3.2 8.0 1.0
PA A:ADP1307 3.2 6.5 1.0
O3A A:ADP1307 3.3 7.6 1.0
O A:HOH2678 3.6 15.4 0.5
O A:HOH2079 3.7 13.7 0.4
NH1 A:ARG21 3.9 7.5 1.0
OD2 A:ASP233 4.0 6.8 1.0
O A:HOH2354 4.1 12.4 0.5
NZ A:LYS217 4.1 7.8 1.0
O2B A:ADP1307 4.1 11.3 1.0
O A:HOH2539 4.1 13.7 1.0
OD1 A:ASP233 4.1 6.8 1.0
O A:HOH2683 4.2 13.0 0.5
O2A A:ADP1307 4.2 6.6 1.0
OE1 A:GLU219 4.2 8.0 1.0
O3B A:ADP1307 4.2 10.4 1.0
O A:HOH2540 4.3 7.7 1.0
O5' A:ADP1307 4.3 6.8 1.0
O A:HOH2078 4.3 11.9 0.5
OE1 A:GLU234 4.4 7.2 1.0
CG A:ASP233 4.5 6.2 1.0
C5' A:ADP1307 4.5 6.9 1.0
O5 A:AMZ1308 4.5 9.5 1.0
NZ A:LYS19 4.6 10.3 0.2
O A:HOH2129 4.6 16.3 0.5
C3' A:ADP1307 4.9 7.2 1.0
O A:HOH2519 4.9 15.1 0.5
O A:HOH2676 5.0 22.5 1.0

Reference:

D.V.Urusova, S.V.Antonyuk, A.I.Grebenko, V.M.Levdikov, V.V.Barynin, A.N.Popov, V.S.Lamzin, W.R.Melik-Adamyan. Saicar Synthase: Substrate Recognition, Conformational Flexibility and Catalysis. To Be Published.
Page generated: Sun Aug 10 10:20:04 2025

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